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Protein

Histone acetyltransferase type B catalytic subunit

Gene

HAT1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei177 – 1771Interaction with histone H4 N-terminusBy similarity
Active sitei258 – 2581Proton donor/acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48By similarity)
Gene namesi
Name:HAT1
Ordered Locus Names:CAGL0L09042g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428 Componenti: Chromosome L

Organism-specific databases

EuPathDBiFungiDB:CAGL0L09042g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Histone acetyltransferase type B catalytic subunitPRO_0000227720Add
BLAST

Interactioni

Subunit structurei

Component of the HAT-B complex composed of at least HAT1 and HAT2. The HAT-B complex binds to histone H4 tail.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6FKS5.
SMRiQ6FKS5. Positions 6-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 306165N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 1993Interaction with histone H4 N-terminusBy similarity
Regioni223 – 2253Acetyl-CoA bindingBy similarity
Regioni230 – 2367Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the HAT1 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiQ6FKS5.
KOiK11303.
OMAiFREYHAR.
OrthoDBiEOG7HTHSD.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FKS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDDFKPEK WTISSNEALK LSLVSEDNAI QFSPTFTYPI FGTEEQIFGY
60 70 80 90 100
KDLVIHLAFD AITFKPFLNV KFSSKFEGSE EELVNIKEKL LEYLPIDDTI
110 120 130 140 150
YKDEEKWIDS FKKEQESIEA YKNDQNIDEY KIDNADFEIY KVNLQDPKMK
160 170 180 190 200
RFHRRIQIFS LLFIEAASYI DEDDPKWEIF IVQTKKDKKF VGYATAYNYW
210 220 230 240 250
YYPGANNFDS ESKYRYRGKI SQFLILPPYQ GRGHGSHLYN SIVKNWRNDS
260 270 280 290 300
SILEIVVEDP NESFDDLRDV NDLEMLYKDG FFNKLPQERP IPNAWIESTR
310 320 330 340 350
LKYKIEKRQF SRLLEMILLS TGSNNFEYQV KQRLLIKNKD GLEGMEVSDI
360 370 380
KDALNKSFES LREDYDRILG KCQFSNDADG PSKKKIKT
Length:388
Mass (Da):45,819
Last modified:July 19, 2004 - v1
Checksum:i7D26B0E7E97840D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380958 Genomic DNA. Translation: CAG62139.1.
RefSeqiXP_449169.1. XM_449169.1.

Genome annotation databases

GeneIDi2891100.
KEGGicgr:CAGL0L09042g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380958 Genomic DNA. Translation: CAG62139.1.
RefSeqiXP_449169.1. XM_449169.1.

3D structure databases

ProteinModelPortaliQ6FKS5.
SMRiQ6FKS5. Positions 6-323.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2891100.
KEGGicgr:CAGL0L09042g.

Organism-specific databases

EuPathDBiFungiDB:CAGL0L09042g.

Phylogenomic databases

InParanoidiQ6FKS5.
KOiK11303.
OMAiFREYHAR.
OrthoDBiEOG7HTHSD.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
PF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHAT1_CANGA
AccessioniPrimary (citable) accession number: Q6FKS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 19, 2004
Last modified: April 29, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.